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5AIO

Crystal structure of t131 N-terminal TPR array

Summary for 5AIO
Entry DOI10.2210/pdb5aio/pdb
Related5AIM
DescriptorTRANSCRIPTION FACTOR TAU 131 KDA SUBUNIT (1 entity in total)
Functional Keywordstranscription, tfiiic, tprs
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
Cellular locationNucleus : P33339
Total number of polymer chains1
Total formula weight52437.97
Authors
Male, G.,Glatt, S.,Mueller, C.W. (deposition date: 2015-02-16, release date: 2015-06-24, Last modification date: 2024-05-08)
Primary citationMale, G.,von Appen, A.,Glatt, S.,Taylor, N.M.,Cristovao, M.,Groetsch, H.,Beck, M.,Muller, C.W.
Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.
Nat Commun, 6:7387-7387, 2015
Cited by
PubMed Abstract: In eukaryotes, RNA Polymerase III (Pol III) is specifically responsible for transcribing genes encoding tRNAs and other short non-coding RNAs. The recruitment of Pol III to tRNA-encoding genes requires the transcription factors (TF) IIIB and IIIC. TFIIIC has been described as a conserved, multi-subunit protein complex composed of two subcomplexes, called τA and τB. How these two subcomplexes are linked and how their interaction affects the formation of the Pol III pre-initiation complex (PIC) is poorly understood. Here we use chemical crosslinking mass spectrometry and determine the molecular architecture of TFIIIC. We further report the crystal structure of the essential TPR array from τA subunit τ131 and characterize its interaction with a central region of τB subunit τ138. The identified τ131-τ138 interacting region is essential in vivo and overlaps with TFIIIB-binding sites, revealing a crucial interaction platform for the regulation of tRNA transcription initiation.
PubMed: 26060179
DOI: 10.1038/ncomms8387
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.148 Å)
Structure validation

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